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Gene Review

ACADM  -  acyl-CoA dehydrogenase, C-4 to C-12...

Sus scrofa

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Disease relevance of ACADM


High impact information on ACADM


Biological context of ACADM


Anatomical context of ACADM


Associations of ACADM with chemical compounds

  • The wild-type enzyme is a yellow protein due to the content of stoichiometric FAD and had a specific activity which is 50% of MCADH purified from pig kidney [1].
  • The large increase in shielding experienced by the C1 and C3 HD carbons in the HD-CoA/MCAD complex is proposed to arise from the ring current field from the isoalloxazine portion of the flavin cofactor [10].
  • These changes in chemical shift are unexpected given the results of previous Raman studies which revealed that the C3=C2-C1=O HD enone fragment is polarized upon binding to MCAD such that the electron density at the C3 and C1 carbons is reduced, not increased (Pellet et al. Biochemistry 2000, 39, 13982-13992) [10].
  • We investigated the influence of Glu-376-->Asp (E376D) mutation on the UV/visible spectral, thermodynamic, and kinetic properties for the interaction of structurally different types of CoA-ligands (viz., octenoyl-CoA, acetoacetyl-CoA, and indoleacryloyl-CoA) to human liver medium-chain acyl-CoA dehydrogenase (MCAD) [11].
  • A series of 8-alkylmercapto-FAD analogues containing increasingly bulky substituents bind tightly to apo-ETF and can be reduced to the dihydroflavin level by octanoyl-CoA in the presence of catalytic levels of the medium-chain acyl-CoA dehydrogenase [12].

Other interactions of ACADM


Analytical, diagnostic and therapeutic context of ACADM


  1. Characterization of wild-type and an active site mutant of human medium chain acyl-CoA dehydrogenase after expression in Escherichia coli. Bross, P., Engst, S., Strauss, A.W., Kelly, D.P., Rasched, I., Ghisla, S. J. Biol. Chem. (1990) [Pubmed]
  2. Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate. Kim, J.J., Wang, M., Paschke, R. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  3. NADPH-dependent beta-oxidation of unsaturated fatty acids with double bonds extending from odd-numbered carbon atoms. Smeland, T.E., Nada, M., Cuebas, D., Schulz, H. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  4. Nucleotide sequence of medium-chain acyl-CoA dehydrogenase mRNA and its expression in enzyme-deficient human tissue. Kelly, D.P., Kim, J.J., Billadello, J.J., Hainline, B.E., Chu, T.W., Strauss, A.W. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  5. Polymorphisms in the promoter region of the porcine acyl-coA dehydrogenase, medium-chain (ACADM) gene have no effect on fat deposition traits in a pig Iberian x Landrace cross. Kim, J.H., Lim, H.T., Park, E.W., Rodríguez, C., Silio, L., Varona, L., Mercade, A., Jeon, J.T., Ovilo, C. Anim. Genet. (2006) [Pubmed]
  6. Influence of alpha-CH-->NH substitution in C8-CoA on the kinetics of association and dissociation of ligands with medium chain acyl-CoA dehydrogenase. Peterson, K.M., Gopalan, K.V., Srivastava, D.K. Biochemistry (2000) [Pubmed]
  7. Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity. Lee, H.J., Wang, M., Paschke, R., Nandy, A., Ghisla, S., Kim, J.J. Biochemistry (1996) [Pubmed]
  8. Identification of the catalytic base in long chain acyl-CoA dehydrogenase. Djordjevic, S., Dong, Y., Paschke, R., Frerman, F.E., Strauss, A.W., Kim, J.J. Biochemistry (1994) [Pubmed]
  9. Purification of electron transfer flavoprotein from pig liver mitochondria and its application to the diagnosis of deficiencies of acyl-CoA dehydrogenases in human fibroblasts. Bertrand, C., Dumoulin, R., Divry, P., Mathieu, M., Vianey-Saban, C. Clin. Chim. Acta (1992) [Pubmed]
  10. Ring current effects in the active site of medium-chain Acyl-CoA dehydrogenase revealed by NMR spectroscopy. Wu, J., Bell, A.F., Jaye, A.A., Tonge, P.J. J. Am. Chem. Soc. (2005) [Pubmed]
  11. Discriminatory influence of Glu-376-->Asp mutation in medium-chain acyl-CoA dehydrogenase on the binding of selected CoA-ligands: spectroscopic, thermodynamic, kinetic, and model building studies. Srivastava, D.K., Peterson, K.L. Biochemistry (1998) [Pubmed]
  12. Electron-transferring flavoprotein from pig kidney: flavin analogue studies. Gorelick, R.J., Thorpe, C. Biochemistry (1986) [Pubmed]
  13. A new form of mammalian electron-transferring flavoprotein. Lehman, T.C., Thorpe, C. Arch. Biochem. Biophys. (1992) [Pubmed]
  14. Elimination reactions in the medium-chain acyl-CoA dehydrogenase: bioactivation of cytotoxic 4-thiaalkanoic acids. Baker-Malcolm, J.F., Haeffner-Gormley, L., Wang, L., Anders, M.W., Thorpe, C. Biochemistry (1998) [Pubmed]
  15. Energetics of two-step binding of a chromophoric reaction product, trans-3-indoleacryloyl-CoA, to medium-chain acyl-coenzyme-A dehydrogenase. Qin, L., Srivastava, D.K. Biochemistry (1998) [Pubmed]
  16. Probing hydrogen-bonding interactions in the active site of medium-chain acyl-CoA dehydrogenase using Raman spectroscopy. Wu, J., Bell, A.F., Luo, L., Stephens, A.W., Stankovich, M.T., Tonge, P.J. Biochemistry (2003) [Pubmed]
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